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Conserved domains on  [gi|1724550794|gb|QEE31136|]
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anti-sigma regulatory factor [Terriglobus albidus]

Protein Classification

anti-sigma regulatory factor( domain architecture ID 13014755)

anti-sigma regulatory factor similar to RsbT, an ATPase with serine/threonine kinase activity that phosphorylates its antagonist RsbS and stimulates the phosphatase RsbU in a signaling cascade that results in active sigma-B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 15-130 3.52e-34

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


:

Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 115.16  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  15 DLVHVRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGGGEMEMSLLAVGARKGIRLKFSDQGPGIADVAMALRDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1724550794  95 YTTAGGMGLGLSGSRRLMSEFDIQSSPGSGTVVTVT 130
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 15-130 3.52e-34

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 115.16  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  15 DLVHVRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGGGEMEMSLLAVGARKGIRLKFSDQGPGIADVAMALRDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1724550794  95 YTTAGGMGLGLSGSRRLMSEFDIQSSPGSGTVVTVT 130
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
15-132 4.45e-18

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  15 DLVHVRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGG----GEMEMSLLAVGARkgIRLKFSDQGPGIAdvAMA 90
Cdd:COG2172    10 DLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPDG--LEIEVRDEGPGFD--PED 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1724550794  91 LRDGYTTAGGMGLGLSGSRRLMSEFDIQSSPGsGTVVTVTRW 132
Cdd:COG2172    86 LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
19-130 7.41e-04

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 36.88  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  19 VRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGGGEME--MSLLAVGARKGIRLKFSDQGPGiADVAMALRDGYT 96
Cdd:pfam13581  11 ARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPEgpVEVRLTSDGGGLVVTVADSGPP-FDPLTLPPPDLE 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1724550794  97 TAGGMGLGL----SGSRRLMSEFDIQSSPGsGTVVTVT 130
Cdd:pfam13581  90 EPDEDRKEGgrglALIRGLMDDVEYTRGGE-GNTVRMR 126
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 35-130 2.55e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 35.32  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794   35 IDQTKIVTAASELARNALEHGG-GGEMEMSLLAVGARkgIRLKFSDQGPGIA--DVAMALRDGYTTAGGMGLG------L 105
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTLERDGDH--VEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIggtglgL 78

                           90       100
                   ....*....|....*....|....*....
gi 1724550794  106 SGSRRLMSEF----DIQSSPGSGTVVTVT 130
Cdd:smart00387  79 SIVKKLVELHggeiSVESEPGGGTTFTIT 107
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 15-130 3.52e-34

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 115.16  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  15 DLVHVRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGGGEMEMSLLAVGARKGIRLKFSDQGPGIADVAMALRDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1724550794  95 YTTAGGMGLGLSGSRRLMSEFDIQSSPGSGTVVTVT 130
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
15-132 4.45e-18

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  15 DLVHVRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGG----GEMEMSLLAVGARkgIRLKFSDQGPGIAdvAMA 90
Cdd:COG2172    10 DLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPDG--LEIEVRDEGPGFD--PED 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1724550794  91 LRDGYTTAGGMGLGLSGSRRLMSEFDIQSSPGsGTVVTVTRW 132
Cdd:COG2172    86 LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
19-130 7.41e-04

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 36.88  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  19 VRQRVRTWLSEERFTLIDQTKIVTAASELARNALEHGGGGEME--MSLLAVGARKGIRLKFSDQGPGiADVAMALRDGYT 96
Cdd:pfam13581  11 ARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPEgpVEVRLTSDGGGLVVTVADSGPP-FDPLTLPPPDLE 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1724550794  97 TAGGMGLGL----SGSRRLMSEFDIQSSPGsGTVVTVT 130
Cdd:pfam13581  90 EPDEDRKEGgrglALIRGLMDDVEYTRGGE-GNTVRMR 126
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 40-83 8.08e-04

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 36.09  E-value: 8.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1724550794  40 IVTAASELARNALEHGG--GGEMEMSLLAVGARKGIRLKFSDQGPG 83
Cdd:cd16936     1 VELAVSEAVTNAVRHAYrhDGPGPVRLELDLDPDRLRVEVTDSGPG 46
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 35-130 2.55e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 35.32  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794   35 IDQTKIVTAASELARNALEHGG-GGEMEMSLLAVGARkgIRLKFSDQGPGIA--DVAMALRDGYTTAGGMGLG------L 105
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTLERDGDH--VEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIggtglgL 78

                           90       100
                   ....*....|....*....|....*....
gi 1724550794  106 SGSRRLMSEF----DIQSSPGSGTVVTVT 130
Cdd:smart00387  79 SIVKKLVELHggeiSVESEPGGGTTFTIT 107
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 33-131 2.78e-03

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 35.59  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  33 TLIDQTKIVTAASELARNALEHGGG--GEMEMSLLAVGARKGIRLKFSDQGPGIADVAMALRDGYTTAGGMGLGL---SG 107
Cdd:cd16942    32 TIDELTEIKTVVSEAVTNAIIHGYNndPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQPLFTTKPELERSGmgfTI 111

                          90       100
                  ....*....|....*....|....
gi 1724550794 108 SRRLMSEFDIQSSPGSGTVVTVTR 131
Cdd:cd16942   112 MENFMDEVIVESEVNKGTTVYLKK 135
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 36-130 3.00e-03

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 35.04  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724550794  36 DQTKIVTAASELARNALEH-GGGGEMEMSLLAVGarkGIRLKFSDQGPGIADVAMA-LRDGYTTAGGMGLG-----LSGS 108
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHaAKAGEITVTLSEGG---ELTLTVEDNGIGIPPEDLPrIFEPFSTADKRGGGgtglgLSIV 78

                          90       100
                  ....*....|....*....|....*.
gi 1724550794 109 RRLMS----EFDIQSSPGSGTVVTVT 130
Cdd:pfam02518  79 RKLVEllggTITVESEPGGGTTVTLT 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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